Matches in Nanopublications for { ?s ?p "We thus investigated the effect of OA, an inhibitor of serine/threonine phosphatases PP1 and PP2A, on ERK2 phosphorylation. In conditions of platelet aggregation, a dose-dependent increase in ERK2 activity was observed in the presence of various concentrations of OA (0?200 nM), with activity reaching 534%�144% (P<0.05) at a concentration of 200 nM (Fig. 2A,E). Moreover, using an anti-T183P antibody, we showed that OA increased ERK2 phosphorylation by 400�133% (P<0.05) at OA concentrations of 200 nM (Fig. 2B,E). In contrast, in the presence of RGDS peptide, in conditions in which ?llb?3 was not engaged, no statistically significant variation in ERK2 activity or in levels of the phosphothreonine form of ERK2 (even at 200 nM OA) was observed ( Fig. 2A,B,F). Surprisingly, increasing the concentration of OA decreased the level of phosphorylation of the Y185 residue of ERK2 (halved at 200 nM OA) in the presence or absence of RGDS peptide (Fig. 2C,E,F). " ?g. }
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- _6 value "We thus investigated the effect of OA, an inhibitor of serine/threonine phosphatases PP1 and PP2A, on ERK2 phosphorylation. In conditions of platelet aggregation, a dose-dependent increase in ERK2 activity was observed in the presence of various concentrations of OA (0?200 nM), with activity reaching 534%�144% (P<0.05) at a concentration of 200 nM (Fig. 2A,E). Moreover, using an anti-T183P antibody, we showed that OA increased ERK2 phosphorylation by 400�133% (P<0.05) at OA concentrations of 200 nM (Fig. 2B,E). In contrast, in the presence of RGDS peptide, in conditions in which ?llb?3 was not engaged, no statistically significant variation in ERK2 activity or in levels of the phosphothreonine form of ERK2 (even at 200 nM OA) was observed ( Fig. 2A,B,F). Surprisingly, increasing the concentration of OA decreased the level of phosphorylation of the Y185 residue of ERK2 (halved at 200 nM OA) in the presence or absence of RGDS peptide (Fig. 2C,E,F). " provenance.
- _6 value "We thus investigated the effect of OA, an inhibitor of serine/threonine phosphatases PP1 and PP2A, on ERK2 phosphorylation. In conditions of platelet aggregation, a dose-dependent increase in ERK2 activity was observed in the presence of various concentrations of OA (0?200 nM), with activity reaching 534%�144% (P<0.05) at a concentration of 200 nM (Fig. 2A,E). Moreover, using an anti-T183P antibody, we showed that OA increased ERK2 phosphorylation by 400�133% (P<0.05) at OA concentrations of 200 nM (Fig. 2B,E). In contrast, in the presence of RGDS peptide, in conditions in which ?llb?3 was not engaged, no statistically significant variation in ERK2 activity or in levels of the phosphothreonine form of ERK2 (even at 200 nM OA) was observed ( Fig. 2A,B,F). Surprisingly, increasing the concentration of OA decreased the level of phosphorylation of the Y185 residue of ERK2 (halved at 200 nM OA) in the presence or absence of RGDS peptide (Fig. 2C,E,F). " provenance.